Title : The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation. Effect of L-Phe and comparison with the rat enzyme.

Pub. Date : 1999 Mar 5

PMID : 10037716






2 Functional Relationships(s)
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1 The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation. Iron phenylalanine hydroxylase Homo sapiens
2 Thus, the recombinant human PAH appears to have a more solvent-accessible catalytic iron than the rat enzyme, in which the water coordinated to the metal is slowly exchanging with the solvent. Iron phenylalanine hydroxylase Homo sapiens